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Solution structure of the oligomerization domain in cep-1

Analyse Solution structure of the oligomerization domain in cep-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2RP5
Type: protein
Length: 234 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative uncharacterized protein cep-1
UniProt: Q20646

Structure

solution nmr · 1 distinct chain · 58% helix, 6% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative uncharacterized protein cep-1	protein	117	58% helix, 6% strand	Q20646

Interfaces

1 interface between chains.

A–B · 1356 Å² buried · 25 hydrogen bonds · protein-protein

Compared structures

2RP5 · Solution structure of the oligomerization domain in CEP-1 · the same entry in another collection · chain A against A, TM-score 1.00
Q20646 · AlphaFold monomer V2.0 prediction for transcription factor cep-1 (Q20646) · a predicted model of the same protein · chain A against A, TM-score 0.75

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q20646
Elsewhere: RCSB PDB 2RP5 · PDBe 2RP5 · UniProt Q20646

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